1AXE
CRYSTAL STRUCTURE OF THE ACTIVE-SITE MUTANT PHE93->TRP OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH NAD AND INHIBITOR TRIFLUOROETHANOL
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Collection date | 1995-09-17 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 1 |
Unit cell lengths | 51.820, 44.580, 93.280 |
Unit cell angles | 103.10, 87.59, 70.55 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ohx |
RMSD bond length | 0.009 |
RMSD bond angle | 24.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 99.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.064 | 0.310 |
Number of reflections | 43756 | |
<I/σ(I)> | 5 | 1.3 |
Completeness [%] | 85.2 | 64.6 |
Redundancy | 1.83 | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8.4 | 4 * | CRYSTALS WERE GROWN FROM HANGING DROPS. THE INITIAL DROP CONTAINING 16MG/ML PROTEIN, A 10X EXCESS OF NAD, 5MM TRIFLUOROETHANOL AND 5% V/V OF PEG400 IN 50MM TRIS-HCL PH 8.4 WERE EQUILIBRATED AT 4 DEGREES C OVER WELLS OF SIMILAR COMPOSITION CONTAINING 15-17% PEG400., vapor diffusion - hanging drop, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16 (mg/ml) | |
2 | 1 | drop | NAD+ | 10 (M) | |
3 | 1 | drop | trifluoroethanol | 5 (mM) | |
4 | 1 | drop | PEG400 | 5 (%(v/v)) | |
5 | 1 | reservoir | Tris-HCl | 50 (mM) | pH8.4 |
6 | 1 | reservoir | trifluoroethanol | 5 (mM) | |
7 | 1 | reservoir | PEG400 | 15-17 (%(v/v)) |